UBP1_RAT
ID UBP1_RAT Reviewed; 784 AA.
AC Q569C3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:O94782};
DE AltName: Full=Deubiquitinating enzyme 1;
DE AltName: Full=Ubiquitin thioesterase 1;
DE AltName: Full=Ubiquitin-specific-processing protease 1;
DE Contains:
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment {ECO:0000250|UniProtKB:O94782};
GN Name=Usp1 {ECO:0000312|EMBL:AAH92574.1, ECO:0000312|RGD:1306461};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH92574.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis {ECO:0000312|EMBL:AAH92574.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Negative regulator of DNA damage repair which specifically
CC deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-
CC mediated translesion synthesis (TLS) by deubiquitinating
CC monoubiquitinated PCNA. Has almost no deubiquitinating activity by
CC itself and requires the interaction with WDR48 to have a high activity.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:O94782};
CC -!- SUBUNIT: Interacts with FANCD2 and PCNA. Interacts with WDR48.
CC Interacts with ATAD5; the interaction regulates USP1-mediated PCNA
CC deubiquitination. {ECO:0000250|UniProtKB:O94782}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94782}.
CC -!- PTM: Autocatalytic cleavage of USP1 following UV irradiation
CC inactivates it leading to an increase in ubiquitinated PCNA,
CC recruitment of POLH and translesion synthesis.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- PTM: [Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment]:
CC Ubiquitinated by the CRL2(KLHDC2) complex following autocatalytic
CC cleavage, leading to its degradation: the CRL2(KLHDC2) complex
CC recognizes the diglycine (Gly-Gly) at the C-terminus.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255}.
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DR EMBL; BC092574; AAH92574.1; -; mRNA.
DR RefSeq; NP_001015015.1; NM_001015015.1.
DR AlphaFoldDB; Q569C3; -.
DR SMR; Q569C3; -.
DR STRING; 10116.ENSRNOP00000010935; -.
DR MEROPS; C19.019; -.
DR iPTMnet; Q569C3; -.
DR PhosphoSitePlus; Q569C3; -.
DR PaxDb; Q569C3; -.
DR PRIDE; Q569C3; -.
DR Ensembl; ENSRNOT00000010933; ENSRNOP00000010935; ENSRNOG00000007890.
DR GeneID; 313387; -.
DR KEGG; rno:313387; -.
DR UCSC; RGD:1306461; rat.
DR CTD; 7398; -.
DR RGD; 1306461; Usp1.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00910000144243; -.
DR HOGENOM; CLU_019874_0_0_1; -.
DR InParanoid; Q569C3; -.
DR OMA; HAIQDVN; -.
DR OrthoDB; 439300at2759; -.
DR PhylomeDB; Q569C3; -.
DR TreeFam; TF331057; -.
DR Reactome; R-RNO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-RNO-6783310; Fanconi Anemia Pathway.
DR PRO; PR:Q569C3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007890; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q569C3; baseline and differential.
DR Genevisible; Q569C3; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02671; Peptidase_C19O; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033815; USP1.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..784
FT /note="Ubiquitin carboxyl-terminal hydrolase 1"
FT /id="PRO_0000306288"
FT CHAIN 1..670
FT /note="Ubiquitin carboxyl-terminal hydrolase 1, N-terminal
FT fragment"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT /id="PRO_0000453164"
FT DOMAIN 81..784
FT /note="USP"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 593
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT SITE 670..671
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJQ2"
SQ SEQUENCE 784 AA; 87329 MW; 4CAFB369297DE7CC CRC64;
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQEDEEKAS EYRGSEIDQV
VPAAQSSPVS CEKRENLLPF VGLNNLGNTC YLNSILQVLY FCPGFKAGVK HLFNIISRKK
EALKDDSIQK DKGSCKEDPL ASYELICSLQ SLIISVEQLQ ASFLLNPEKY TDELATQPRR
LLNTLRELNP MYEGYLQHDA QEVLQCILGN IQETCQLLKK EEIKNLTEFS SKVEEKSLQK
EETGGISSTE TDSTRNLDDL KEQLPKGNWK RKSDGESGNM KKKVKLSRES QPLEENQRQT
RSKRKATGDT LEASPKIIPK CVSENESAKP SQKKSKVKIN WLKPATKQPS ILSKFCSLGK
ITTNQRSKGQ PKVNEGDLEE DLEKDGRDNT VNGSGPASPG SSVTPVDSSE AKSINKGAEQ
IGFELVEKLF QGQLVLRTRC LECESLTERR EDFQDISVPV QEDELSKVEE SSEISPEPKT
EMKTLRWAIS QFASVERIVG EDKYFCENCH HYTEAERSLL FDKMPEVITI HLKCFAASGL
EFDCYGGGLS KINTPLLTPL KLSLEEWSTK PTNDSYGLFA VVMHSGITIS SGHYTASVKV
TDLNSLELDK GNFVVDQMCE IGKPEPLNEE EARGTAENYD DEVSIRVGGN AQPSKVLNKK
NVEGIGLLGG QKSKADYELC SKASNPEKVV GTPFTDSRNS ETNDTNGTQE SDRSKESSDQ
TGINVSGLEN KISYVVQSLK EYEGKWLLFD DSEVKVTEEK DFLNSLSPST SPTSTPYLLF
YKKL
